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Protein

Aldose reductase

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Alditol + NAD(P)+ = aldose + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei60 – 601Proton donorBy similarity
Sitei88 – 881Lowers pKa of active site TyrBy similarity
Binding sitei121 – 1211SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi215 – 26955NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB-EC

GO - Biological processi

  1. photoperiodism, flowering Source: EnsemblPlants/Gramene
  2. vernalization response Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Aldose reductase (EC:1.1.1.21)
Short name:
AR
Alternative name(s):
Aldehyde reductase
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Organism-specific databases

GrameneiP23901.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320Aldose reductasePRO_0000124628Add
BLAST

Expressioni

Inductioni

By abscisic acid (ABA) and gibberellic acid (GA).

Gene expression databases

ExpressionAtlasiP23901. baseline.
GenevestigatoriP23901.

Structurei

Secondary structure

1
320
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 173Combined sources
Beta strandi23 – 275Combined sources
Helixi35 – 373Combined sources
Helixi38 – 4710Combined sources
Beta strandi53 – 553Combined sources
Helixi58 – 603Combined sources
Helixi63 – 7513Combined sources
Helixi80 – 823Combined sources
Beta strandi84 – 896Combined sources
Helixi91 – 933Combined sources
Helixi96 – 983Combined sources
Helixi99 – 11012Combined sources
Beta strandi115 – 1239Combined sources
Helixi144 – 15613Combined sources
Beta strandi159 – 1679Combined sources
Helixi170 – 17910Combined sources
Beta strandi185 – 1906Combined sources
Helixi198 – 2069Combined sources
Beta strandi210 – 2156Combined sources
Turni219 – 2224Combined sources
Helixi224 – 2263Combined sources
Helixi228 – 23710Combined sources
Helixi241 – 25212Combined sources
Beta strandi255 – 2573Combined sources
Helixi263 – 2686Combined sources
Helixi279 – 2879Combined sources
Helixi298 – 3014Combined sources
Turni304 – 3063Combined sources
Helixi312 – 3154Combined sources
Turni316 – 3183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BGQX-ray2.50A2-320[»]
2BGSX-ray1.64A2-320[»]
2VDGX-ray1.92A2-320[»]
ProteinModelPortaliP23901.
SMRiP23901. Positions 13-320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23901.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASAKATMGQ GEQDHFVLKS GHAMPAVGLG TWRAGSDTAH SVRTAITEAG
60 70 80 90 100
YRHVDTAAEY GVEKEVGKGL KAAMEAGIDR KDLFVTSKIW CTNLAPERVR
110 120 130 140 150
PALENTLKDL QLDYIDLYHI HWPFRLKDGA HMPPEAGEVL EFDMEGVWKE
160 170 180 190 200
MENLVKDGLV KDIGVCNYTV TKLNRLLRSA KIPPAVCQME MHPGWKNDKI
210 220 230 240 250
FEACKKHGIH VTAYSPLGSS EKNLAHDPVV EKVANKLNKT PGQVLIKWAL
260 270 280 290 300
QRGTSVIPKS SKDERIKENI QVFGWEIPEE DFKVLCSIKD EKRVLTGEEL
310 320
FVNKTHGPYR SAADVWDHEN
Length:320
Mass (Da):35,807
Last modified:November 1, 1991 - v1
Checksum:i5AA72C021E9A93C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57526 Genomic DNA. Translation: CAA40747.1.
PIRiS15024.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57526 Genomic DNA. Translation: CAA40747.1.
PIRiS15024.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BGQX-ray2.50A2-320[»]
2BGSX-ray1.64A2-320[»]
2VDGX-ray1.92A2-320[»]
ProteinModelPortaliP23901.
SMRiP23901. Positions 13-320.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiP23901.

Miscellaneous databases

EvolutionaryTraceiP23901.

Gene expression databases

ExpressionAtlasiP23901. baseline.
GenevestigatoriP23901.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "An ABA and GA modulated gene expressed in the barley embryo encodes an aldose reductase related protein."
    Bartels D., Engelhardt K., Roncarati R., Schneider K., Rotter M., Salamini F.
    EMBO J. 10:1037-1043(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Aura.
  2. "Barley aldose reductase: structure, cofactor binding, and substrate recognition in the aldo/keto reductase 4C family."
    Olsen J.G., Pedersen L., Christensen C.L., Olsen O., Henriksen A.
    Proteins 71:1572-1581(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 2-320.

Entry informationi

Entry nameiALDR_HORVU
AccessioniPrimary (citable) accession number: P23901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: January 7, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.